Maltose Separopore® 4B (Epoxy-Coupled)

Applications

Maltose is coupled with Separopore® 4B. Maltose Separopore® 4B provides a convenient affinity purification of recombinant proteins tagged with maltose-binding protein (MBP). Maltose Separopore® 4B has high binding capacity for MBP-tagged proteins. Purification is performed under physiological conditions and the mild elution preserves the activity of the target protein. Due to the high specificity of the binding, very high purity of the eluted protein is achieved in just one step. Maltose-Separopore® 4B is used in protein chromatography, affinity chromatography and carbohydrate matrices. Maltose-Separopore® 4B has been used to study surfactant protein D (SP-D), which plays an important role in innate immunity. Maltose-Separopore® 4B has also been used to study numerous pathological mechanisms for diseases in the human lung, including Aspergillus fumigatus, a pathogenic fungus, and the human influenza A virus.

Note: Separopore® is a cost-effective equivalent to Sepharose® in all of its physical properties and binding characteristics.

References

Purification, characterization and immunolocalization of porcine surfactant protein D. Immunology. (2005) 114: 72-82. Identification and characterization of a novel interaction between pulmonary surfactant protein D and decorin. J Biol Chem. (2003) 278: 25678-87. Enhanced binding of Aspergillus fumigates spores to A549 epithelial cells and extracellular matrix proteins by a component from the spore surface and inhibition by rat lung lavage fluid. Thorax. (2000) 55: 579-84. Structure of a truncated human surfactant protein D is less effective in agglutinating bacteria than the native structure and fails to inhibit haemagglutination by influenza A virus. Biochem J. (1997) 323: 393-9. The alpha-helical neck region of human lung surfactant protein D is essential for the binding of the carbohydrate recognition domains to lipopolysaccharides and phospholipids. Biochem J. (1996) 318: 505-11. Mite allergen induces nitric oxide production in alveolar macrophage cell lines via CD14/toll-like receptor 4, and is inhibited by surfactant protein D. Clin Exp Allergy. (2005) 35: 1615-24. Purification, characterization and cDNA cloning of human lung surfactant protein D. Biochem J. (1992) 284: 795-802.